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Database: UniProt
Entry: D0SUA7_ACILW
LinkDB: D0SUA7_ACILW
Original site: D0SUA7_ACILW 
ID   D0SUA7_ACILW            Unreviewed;       301 AA.
AC   D0SUA7;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=TIGR01777 family protein {ECO:0000313|EMBL:EEY90462.1};
GN   ORFNames=HMPREF0017_00881 {ECO:0000313|EMBL:EEY90462.1};
OS   Acinetobacter lwoffii SH145.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=575588 {ECO:0000313|EMBL:EEY90462.1, ECO:0000313|Proteomes:UP000018425};
RN   [1] {ECO:0000313|Proteomes:UP000018425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH145 {ECO:0000313|Proteomes:UP000018425};
RX   PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA   Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA   Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA   Seifert H., Dijkshoorn L.;
RT   "The success of Acinetobacter species; genetic, metabolic and virulence
RT   attributes.";
RL   PLoS ONE 7:E46984-E46984(2012).
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. SDR39U1 subfamily. {ECO:0000256|ARBA:ARBA00009353}.
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DR   EMBL; GG705057; EEY90462.1; -; Genomic_DNA.
DR   RefSeq; WP_004279286.1; NZ_GG705057.1.
DR   AlphaFoldDB; D0SUA7; -.
DR   eggNOG; COG1090; Bacteria.
DR   HOGENOM; CLU_047373_0_3_6; -.
DR   Proteomes; UP000018425; Unassembled WGS sequence.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013549; DUF1731.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR010099; SDR39U1.
DR   NCBIfam; TIGR01777; yfcH; 1.
DR   PANTHER; PTHR11092:SF0; EPIMERASE FAMILY PROTEIN SDR39U1; 1.
DR   PANTHER; PTHR11092; SUGAR NUCLEOTIDE EPIMERASE RELATED; 1.
DR   Pfam; PF08338; DUF1731; 1.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
FT   DOMAIN          6..225
FT                   /note="NAD-dependent epimerase/dehydratase"
FT                   /evidence="ECO:0000259|Pfam:PF01370"
FT   DOMAIN          253..298
FT                   /note="DUF1731"
FT                   /evidence="ECO:0000259|Pfam:PF08338"
SQ   SEQUENCE   301 AA;  34526 MW;  AC920B228030E488 CRC64;
     MYKPVVLLTG ASGFIGSHLV HFLLERDYRV IGLTRQKNKR EPHPDFHWIN QLDELKQHQI
     DYVVNLAGES IGQGRWTAAR KKKLLNSRLD TTRHLFDYLE KNQLRPKRII STSAVGYYGI
     DPNERWEQVC TEQSPPQDIF MSELCAKWEQ LALSYANQNT KIVRFAVVFG KGGGILPQML
     LPIKLNLFGR IGHGRQPVTW VYLEDVLRAI EFLMLDDTTE QIFNVVAPEK SSQAQFARTA
     AQILKRKPLF PLPACSLKMM LGEQSQLVLN GQYVQPKALQ EAGFQFHYPT LKEALDNILK
     H
//
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